Results 21 to 30 of about 80,914 (291)

Pyruvate Dehydrogenase Kinase 4 [PDF]

Diabetes, 2008
OBJECTIVE—Pyruvate dehydrogenase complex (PDC) serves as the metabolic switch between glucose and fatty acid utilization. PDC activity is inhibited by PDC kinase (PDK). PDC shares the same substrate, i.e., pyruvate, as glyceroneogenesis, a pathway controlling fatty acid release from white adipose tissue (WAT).
Thomas Cadoudal, Emilie Distel, Sylvie Durant, Françoise Fouque, Jean-Marc Blouin, Martine Collinet, Sylvie Bortoli, Claude Forest, Chantal Benelli   +8 more
openaire   +1 more source

Variation in the organization and subunit composition of the mammalian pyruvate dehydrogenase complex E2/E3BP core assembly [PDF]

, 2011
Crucial to glucose homoeostasis in humans, the hPDC (human pyruvate dehydrogenase complex) is a massive molecular machine comprising multiple copies of three distinct enzymes (E1–E3) and an accessory subunit, E3BP (E3-binding protein). Its icosahedral E2/
Swetha Vijayakrishnan, Byron, Olwyn, Lindsay, J., Gilbert, David, Cooper, Alan, Lindsay, J.G., Nutley, Margaret A, Philip Callow, Byron, O., Callow, P, David Gilbert, Kropholler, P., Callow, Philip, Byron, O, McGow, D., Vijayakrishnan, S, David, Gilbert, Vijayakrishnan, Swetha, McGow, Donna P., Nutley, M.A., Gilbert, D, Callow, P., Kropholler, P, Alan Cooper, Nutley, Margaret A., Cooper, A., Donna P. McGow, Lindsay, J Gordon, Nutley, M., Lindsay, J. Gordon, Cooper, A, J. Gordon Lindsay, Vijayakrishnan, S., McGow, DP, Margaret A. Nutley, Olwyn Byron, Kropholler, Peter, Peter Kropholler, Mcgow, Donna P, Lindsay, JG, Nutley, MA, McGow, D.P., Gilbert, D.   +42 more
core   +1 more source

Hyperpolarized NMR study of the impact of pyruvate dehydrogenase kinase inhibition on the pyruvate dehydrogenase and TCA flux in type 2 diabetic rat muscle [PDF]

, 2021
The role of pyruvate dehydrogenase in mediating lipid-induced insulin resistance stands as a central question in the pathogenesis of type 2 diabetes mellitus.
Hurd, Ralph E, Hurd, Ralph E., Josan, Sonal, Mayer, Dirk, Havel, Peter, Spielman, Daniel M, Hurd, Ralph, Park, Jae Mo, Chung, Youngran, Spielman, Daniel, Bendahan, David, Havel, Peter J, Havel, Peter J., Spielman, Daniel M., Graham, James, Jue, Thomas   +15 more
core   +1 more source

Scanning mutagenesis of the amino acid sequences flanking phosphorylation site 1 of the mitochondrial pyruvate dehydrogenase complex

Frontiers in Plant Science, 2012
The mitochondrial pyruvate dehydrogenase complex is regulated by reversible seryl-phosphorylation of the E1α subunit by a dedicated, intrinsic kinase. The phospho-complex is reactivated when dephosphorylated by an intrinsic PP2C-type protein phosphatase.
Nagib eAhsan, Kirby eSwatek, Jingfen eZhang, Ján Andrew Miernyk, Dong eXu, Jay eThelen   +5 more
doaj   +1 more source

Metabolic checkpoint of ferroptosis resistance

Molecular & Cellular Oncology, 2021
The metabolic checkpoint of ferroptosis remains obscure. We find that glucose favors system xc− inhibitor-induced ferroptosis by activating pyruvate oxidation, thereby promoting fatty acid synthesis and subsequent lipid peroxidation.
Jiao Liu, Rui Kang, Daolin Tang
doaj   +1 more source

Metabolic responses of primary and transformed cells to intracellular Listeria monocytogenes. [PDF]

, 2012
The metabolic response of host cells, in particular of primary mammalian cells, to bacterial infections is poorly understood. Here, we compare the carbon metabolism of primary mouse macrophages and of established J774A.1 cells upon Listeria monocytogenes
Wolfgang Eisenreich (108576), Anette Schulz (108573), Andreas Götz (108569), Gillmaier, Nadine, Götz, Andreas, Nadine Gillmaier, Schulz, Anette, Werner Goebel, Goebel, Werner, Eisenreich, Wolfgang, Werner Goebel (7241), Andreas Götz, Anette Schulz, Wolfgang Eisenreich, Nadine Gillmaier (108566)   +14 more
core   +1 more source

Regulation of heart muscle pyruvate dehydrogenase kinase [PDF]

Biochemical Journal, 1974
1. The activity of pig heart pyruvate dehydrogenase kinase was assayed by the incorporation of [32P]phosphate from [γ-32P]ATP into the dehydrogenase complex. There was a very close correlation between this incorporation and the loss of pyruvate dehydrogenase activity with all preparations studied. 2.
R H, Cooper, P J, Randle, R M, Denton
openaire   +2 more sources

Allosteric Coupling in Pyruvate Dehydrogenase Kinase 2 [PDF]

Biochemistry, 2008
Mitochondrial pyruvate dehydrogenase kinase 2 (PDHK2) phosphorylates the pyruvate dehydrogenase multienzyme complex (PDC) and thereby controls the rate of oxidative decarboxylation of pyruvate. The activity of PDHK2 is regulated by a variety of metabolites such as pyruvate, NAD (+), NADH, CoA, and acetyl-CoA.
Alla, Klyuyeva, Alina, Tuganova, Kirill M, Popov   +2 more
openaire   +2 more sources

Bortezomib-induced aerobic glycolysis contributes to chemotherapy-induced painful peripheral neuropathy

Molecular Pain, 2019
Chemotherapy-induced painful peripheral neuropathy (CIPN) is the most common toxicity associated with widely used chemotherapeutics. CIPN is the major cause of dose reduction or discontinuation of otherwise life-saving treatment.
Taylor Ludman, Ohannes K. Melemedjian
doaj   +1 more source

PDK4 dictates metabolic resistance to ferroptosis by suppressing pyruvate oxidation and fatty acid synthesis

Cell Reports, 2021
Summary: Although induction of ferroptosis, an iron-dependent form of non-apoptotic cell death, has emerged as an anticancer strategy, the metabolic basis of ferroptotic death remains poorly elucidated.
Xinxin Song, Jiao Liu, Feimei Kuang, Xin Chen, Herbert J. Zeh, III, Rui Kang, Guido Kroemer, Yangchun Xie, Daolin Tang   +8 more
doaj   +1 more source